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The RGD containing site of the mouse laminin A chain is active for cell attachment, spreading, migration and neurite outgrowth
Author(s) -
Tashiro KenIchiro,
Sephel Gregory C.,
Greatorex Dave,
Sasaki Makoto,
Shirashi Norio,
Martin George R.,
Kleinman Hynda K.,
Yamada Yoshihiko
Publication year - 1991
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041460316
Subject(s) - laminin , fibronectin , integrin , neurite , cell adhesion , microbiology and biotechnology , complementary dna , chemistry , adhesion , receptor , biology , cell , biochemistry , extracellular matrix , in vitro , gene , organic chemistry
The laminin A chain has been sequenced by cDNA cloning and was found to contain an RGD sequence. Synthetic peptides containing the RGD sequence and flanking amino acids were active in mediating cell adhesion, spreading, migration, and neurite outgrowth. Furthermore, endothelial cell attachment to a laminin substrate was inhibited by an RGD‐containing synthetic peptide. Antisera against the integrin (fibronectin) receptor, and monoclonal antibody to the integrin, VLA‐6, inhibited cell interaction with laminin, as well as with peptides containing an RGD sequence. These results suggest that the RGD containing site of laminin is active and interacts with the integrin family of receptors in certain cells.